Spt5 histone binding activity preserves chromatin during transcription by RNA polymerase II

Cecile Evrin, Albert Serra-Cardona, Shoufu Duan, Progya P. Mukherjee, Zhiguo Zhang (Lead / Corresponding author), Karim P. M. Labib (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)
70 Downloads (Pure)

Abstract

Nucleosomes are disrupted transiently during eukaryotic transcription, yet the displaced histones must be retained and redeposited onto DNA, to preserve nucleosome density and associated histone modifications. Here we show that the essential Spt5 processivity factor of RNA polymerase II (Pol II) plays a direct role in this process in budding yeast. Functional orthologues of eukaryotic Spt5 are present in archaea and bacteria, reflecting its universal role in RNA polymerase processivity. However, eukaryotic Spt5 is unique in having an acidic amino terminal tail (Spt5N) that is sandwiched between the downstream nucleosome and the upstream DNA that emerges from Pol II. We show that Spt5N contains a histone-binding motif that is required for viability in yeast cells and prevents loss of nucleosomal histones within actively transcribed regions. These findings indicate that eukaryotic Spt5 combines two essential activities, which together couple processive transcription to the efficient capture and re-deposition of nucleosomal histones
Original languageEnglish
Article numbere109783
Pages (from-to)1-14
Number of pages14
JournalEMBO Journal
Volume41
Issue number5
Early online date1 Feb 2022
DOIs
Publication statusPublished - 1 Mar 2022

Keywords

  • Spt5
  • transcription
  • chromatin
  • RNA polymerase II
  • Histone
  • histone

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